HEADER OXIDOREDUCTASE 06-JAN-00 1DR0
TITLE STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-
TITLE 2 TERMINUS, HD708
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-ISOPROPYLMALATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IPMDH, IMDH;
COMPND 5 EC: 1.1.1.85;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: LEUB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS DEHYDROGENASE, MINOR GROOVE, PAPERCLIP MOTION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.NURACHMAN,S.AKANUMA,T.SATO,T.OSHIMA,N.TANAKA
REVDAT 6 09-AUG-23 1DR0 1 REMARK
REVDAT 5 04-OCT-17 1DR0 1 REMARK
REVDAT 4 13-JUL-11 1DR0 1 VERSN
REVDAT 3 24-FEB-09 1DR0 1 VERSN
REVDAT 2 31-MAY-00 1DR0 1 JRNL
REVDAT 1 19-JAN-00 1DR0 0
JRNL AUTH Z.NURACHMAN,S.AKANUMA,T.SATO,T.OSHIMA,N.TANAKA
JRNL TITL CRYSTAL STRUCTURES OF 3-ISOPROPYLMALATE DEHYDROGENASES WITH
JRNL TITL 2 MUTATIONS AT THE C-TERMINUS: CRYSTALLOGRAPHIC ANALYSES OF
JRNL TITL 3 STRUCTURE-STABILITY RELATIONSHIPS.
JRNL REF PROTEIN ENG. V. 13 253 2000
JRNL REFN ISSN 0269-2139
JRNL PMID 10810156
JRNL DOI 10.1093/PROTEIN/13.4.253
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR (ONLINE) 98.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 7949325.340
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.6
REMARK 3 NUMBER OF REFLECTIONS : 27745
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2765
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3468
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 381
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5188
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.34
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 28.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 17.16
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.610 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.620 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 25.430; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 24.120; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.PARAM
REMARK 3 TOPOLOGY FILE 3 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 4 : PROTEIN.LINK
REMARK 3 TOPOLOGY FILE 5 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010312.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39276
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 54.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 64.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: IPMDH A171L (PDB 1OSJ)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, SODIUM ACETATE, PH 4.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 42.15500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER FROM CHAIN A AND
REMARK 300 CHAIN B
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 406 O HOH B 418 0.98
REMARK 500 O HOH A 388 O HOH A 406 1.91
REMARK 500 O PRO A 75 OD1 ASP A 78 2.17
REMARK 500 OG SER B 116 O LEU B 250 2.18
REMARK 500 NZ LYS A 310 O VAL A 344 2.19
REMARK 500 NH1 ARG B 176 OD1 ASP B 231 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 352 O HOH B 364 2856 1.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 49 -8.47 -155.04
REMARK 500 PHE A 53 72.46 -114.37
REMARK 500 LYS A 83 14.89 -69.99
REMARK 500 ILE A 84 2.48 -150.70
REMARK 500 ASP A 127 73.47 -167.47
REMARK 500 ARG A 176 -124.62 -120.01
REMARK 500 VAL A 188 -25.53 -152.17
REMARK 500 ALA A 228 -8.90 -56.25
REMARK 500 ASP A 231 -84.09 -115.55
REMARK 500 SER A 253 124.11 174.60
REMARK 500 ASP A 278 -9.40 -52.19
REMARK 500 ALA A 285 129.70 -33.79
REMARK 500 LEU A 304 44.98 -99.53
REMARK 500 VAL A 305 -61.41 -29.70
REMARK 500 ASP A 326 -3.10 -57.09
REMARK 500 PHE B 49 -17.78 -146.52
REMARK 500 ASP B 98 50.72 39.60
REMARK 500 ASP B 127 68.49 -159.62
REMARK 500 ARG B 176 -112.68 -115.38
REMARK 500 VAL B 188 -33.40 -155.35
REMARK 500 SER B 226 68.97 -154.84
REMARK 500 ASP B 231 -86.35 -115.17
REMARK 500 SER B 253 119.50 -176.88
REMARK 500 ALA B 276 59.75 39.77
REMARK 500 GLU B 299 -70.93 -58.04
REMARK 500 ASP B 326 2.13 -67.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OSJ RELATED DB: PDB
REMARK 900 MODIFIED 1OSJ AT THE C-TERMINUS
REMARK 900 RELATED ID: 1DPZ RELATED DB: PDB
REMARK 900 PARTLY RESTORED THERMAL STABILITY MUTANT
REMARK 900 RELATED ID: 1DR8 RELATED DB: PDB
REMARK 900 PARTLY RESTORED THERMAL STABILITY MUTANT
DBREF 1DR0 A 1 345 UNP Q5SIY4 Q5SIY4_THET8 1 345
DBREF 1DR0 B 1 345 UNP Q5SIY4 Q5SIY4_THET8 1 345
SEQADV 1DR0 ARG A 85 UNP Q5SIY4 SER 85 SEE REMARK 999
SEQADV 1DR0 LEU A 172 UNP Q5SIY4 ALA 172 SEE REMARK 999
SEQADV 1DR0 THR A 341 UNP Q5SIY4 LEU 341 SEE REMARK 999
SEQADV 1DR0 ALA A 342 UNP Q5SIY4 ARG 342 SEE REMARK 999
SEQADV 1DR0 THR A 343 UNP Q5SIY4 HIS 343 SEE REMARK 999
SEQADV 1DR0 VAL A 344 UNP Q5SIY4 LEU 344 SEE REMARK 999
SEQADV 1DR0 GLY A 345 UNP Q5SIY4 ALA 345 SEE REMARK 999
SEQADV 1DR0 ILE A 346 UNP Q5SIY4 SEE REMARK 999
SEQADV 1DR0 ARG B 85 UNP Q5SIY4 SER 85 SEE REMARK 999
SEQADV 1DR0 LEU B 172 UNP Q5SIY4 ALA 172 SEE REMARK 999
SEQADV 1DR0 THR B 341 UNP Q5SIY4 LEU 341 SEE REMARK 999
SEQADV 1DR0 ALA B 342 UNP Q5SIY4 ARG 342 SEE REMARK 999
SEQADV 1DR0 THR B 343 UNP Q5SIY4 HIS 343 SEE REMARK 999
SEQADV 1DR0 VAL B 344 UNP Q5SIY4 LEU 344 SEE REMARK 999
SEQADV 1DR0 GLY B 345 UNP Q5SIY4 ALA 345 SEE REMARK 999
SEQADV 1DR0 ILE B 346 UNP Q5SIY4 SEE REMARK 999
SEQRES 1 A 346 MET LYS VAL ALA VAL LEU PRO GLY ASP GLY ILE GLY PRO
SEQRES 2 A 346 GLU VAL THR GLU ALA ALA LEU LYS VAL LEU ARG ALA LEU
SEQRES 3 A 346 ASP GLU ALA GLU GLY LEU GLY LEU ALA TYR GLU VAL PHE
SEQRES 4 A 346 PRO PHE GLY GLY ALA ALA ILE ASP ALA PHE GLY GLU PRO
SEQRES 5 A 346 PHE PRO GLU PRO THR ARG LYS GLY VAL GLU GLU ALA GLU
SEQRES 6 A 346 ALA VAL LEU LEU GLY SER VAL GLY GLY PRO LYS TRP ASP
SEQRES 7 A 346 GLY LEU PRO ARG LYS ILE ARG PRO GLU THR GLY LEU LEU
SEQRES 8 A 346 SER LEU ARG LYS SER GLN ASP LEU PHE ALA ASN LEU ARG
SEQRES 9 A 346 PRO ALA LYS VAL PHE PRO GLY LEU GLU ARG LEU SER PRO
SEQRES 10 A 346 LEU LYS GLU GLU ILE ALA ARG GLY VAL ASP VAL LEU ILE
SEQRES 11 A 346 VAL ARG GLU LEU THR GLY GLY ILE TYR PHE GLY GLU PRO
SEQRES 12 A 346 ARG GLY MET SER GLU ALA GLU ALA TRP ASN THR GLU ARG
SEQRES 13 A 346 TYR SER LYS PRO GLU VAL GLU ARG VAL ALA ARG VAL ALA
SEQRES 14 A 346 PHE GLU LEU ALA ARG LYS ARG ARG LYS HIS VAL VAL SER
SEQRES 15 A 346 VAL ASP LYS ALA ASN VAL LEU GLU VAL GLY GLU PHE TRP
SEQRES 16 A 346 ARG LYS THR VAL GLU GLU VAL GLY ARG GLY TYR PRO ASP
SEQRES 17 A 346 VAL ALA LEU GLU HIS GLN TYR VAL ASP ALA MET ALA MET
SEQRES 18 A 346 HIS LEU VAL ARG SER PRO ALA ARG PHE ASP VAL VAL VAL
SEQRES 19 A 346 THR GLY ASN ILE PHE GLY ASP ILE LEU SER ASP LEU ALA
SEQRES 20 A 346 SER VAL LEU PRO GLY SER LEU GLY LEU LEU PRO SER ALA
SEQRES 21 A 346 SER LEU GLY ARG GLY THR PRO VAL PHE GLU PRO VAL HIS
SEQRES 22 A 346 GLY SER ALA PRO ASP ILE ALA GLY LYS GLY ILE ALA ASN
SEQRES 23 A 346 PRO THR ALA ALA ILE LEU SER ALA ALA MET MET LEU GLU
SEQRES 24 A 346 HIS ALA PHE GLY LEU VAL GLU LEU ALA ARG LYS VAL GLU
SEQRES 25 A 346 ASP ALA VAL ALA LYS ALA LEU LEU GLU THR PRO PRO PRO
SEQRES 26 A 346 ASP LEU GLY GLY SER ALA GLY THR GLU ALA PHE THR ALA
SEQRES 27 A 346 THR VAL THR ALA THR VAL GLY ILE
SEQRES 1 B 346 MET LYS VAL ALA VAL LEU PRO GLY ASP GLY ILE GLY PRO
SEQRES 2 B 346 GLU VAL THR GLU ALA ALA LEU LYS VAL LEU ARG ALA LEU
SEQRES 3 B 346 ASP GLU ALA GLU GLY LEU GLY LEU ALA TYR GLU VAL PHE
SEQRES 4 B 346 PRO PHE GLY GLY ALA ALA ILE ASP ALA PHE GLY GLU PRO
SEQRES 5 B 346 PHE PRO GLU PRO THR ARG LYS GLY VAL GLU GLU ALA GLU
SEQRES 6 B 346 ALA VAL LEU LEU GLY SER VAL GLY GLY PRO LYS TRP ASP
SEQRES 7 B 346 GLY LEU PRO ARG LYS ILE ARG PRO GLU THR GLY LEU LEU
SEQRES 8 B 346 SER LEU ARG LYS SER GLN ASP LEU PHE ALA ASN LEU ARG
SEQRES 9 B 346 PRO ALA LYS VAL PHE PRO GLY LEU GLU ARG LEU SER PRO
SEQRES 10 B 346 LEU LYS GLU GLU ILE ALA ARG GLY VAL ASP VAL LEU ILE
SEQRES 11 B 346 VAL ARG GLU LEU THR GLY GLY ILE TYR PHE GLY GLU PRO
SEQRES 12 B 346 ARG GLY MET SER GLU ALA GLU ALA TRP ASN THR GLU ARG
SEQRES 13 B 346 TYR SER LYS PRO GLU VAL GLU ARG VAL ALA ARG VAL ALA
SEQRES 14 B 346 PHE GLU LEU ALA ARG LYS ARG ARG LYS HIS VAL VAL SER
SEQRES 15 B 346 VAL ASP LYS ALA ASN VAL LEU GLU VAL GLY GLU PHE TRP
SEQRES 16 B 346 ARG LYS THR VAL GLU GLU VAL GLY ARG GLY TYR PRO ASP
SEQRES 17 B 346 VAL ALA LEU GLU HIS GLN TYR VAL ASP ALA MET ALA MET
SEQRES 18 B 346 HIS LEU VAL ARG SER PRO ALA ARG PHE ASP VAL VAL VAL
SEQRES 19 B 346 THR GLY ASN ILE PHE GLY ASP ILE LEU SER ASP LEU ALA
SEQRES 20 B 346 SER VAL LEU PRO GLY SER LEU GLY LEU LEU PRO SER ALA
SEQRES 21 B 346 SER LEU GLY ARG GLY THR PRO VAL PHE GLU PRO VAL HIS
SEQRES 22 B 346 GLY SER ALA PRO ASP ILE ALA GLY LYS GLY ILE ALA ASN
SEQRES 23 B 346 PRO THR ALA ALA ILE LEU SER ALA ALA MET MET LEU GLU
SEQRES 24 B 346 HIS ALA PHE GLY LEU VAL GLU LEU ALA ARG LYS VAL GLU
SEQRES 25 B 346 ASP ALA VAL ALA LYS ALA LEU LEU GLU THR PRO PRO PRO
SEQRES 26 B 346 ASP LEU GLY GLY SER ALA GLY THR GLU ALA PHE THR ALA
SEQRES 27 B 346 THR VAL THR ALA THR VAL GLY ILE
FORMUL 3 HOH *143(H2 O)
HELIX 1 1 ILE A 11 GLY A 31 1 21
HELIX 2 2 GLY A 42 GLY A 50 1 9
HELIX 3 3 PRO A 54 GLU A 63 1 10
HELIX 4 4 PRO A 81 ILE A 84 5 4
HELIX 5 5 ARG A 85 GLN A 97 1 13
HELIX 6 6 LEU A 112 SER A 116 5 5
HELIX 7 7 LYS A 119 ARG A 124 1 6
HELIX 8 8 LYS A 159 LYS A 175 1 17
HELIX 9 9 LEU A 189 GLY A 205 1 17
HELIX 10 10 VAL A 216 SER A 226 1 11
HELIX 11 11 PRO A 227 PHE A 230 5 4
HELIX 12 12 GLY A 236 LEU A 250 1 15
HELIX 13 13 SER A 253 LEU A 256 5 4
HELIX 14 14 ALA A 276 ALA A 280 5 5
HELIX 15 15 PRO A 287 GLY A 303 1 17
HELIX 16 16 LEU A 304 THR A 322 1 19
HELIX 17 17 PRO A 324 GLY A 328 5 5
HELIX 18 18 GLY A 332 ILE A 346 1 15
HELIX 19 19 ILE B 11 ALA B 29 1 19
HELIX 20 20 GLY B 42 GLY B 50 1 9
HELIX 21 21 PRO B 54 ALA B 64 1 11
HELIX 22 22 GLY B 74 GLY B 79 1 6
HELIX 23 23 PRO B 81 ILE B 84 5 4
HELIX 24 24 ARG B 85 GLN B 97 1 13
HELIX 25 25 LYS B 119 ARG B 124 1 6
HELIX 26 26 LYS B 159 LYS B 175 1 17
HELIX 27 27 LEU B 189 ARG B 204 1 16
HELIX 28 28 VAL B 216 SER B 226 1 11
HELIX 29 29 PRO B 227 PHE B 230 5 4
HELIX 30 30 GLY B 236 VAL B 249 1 14
HELIX 31 31 SER B 253 LEU B 257 5 5
HELIX 32 32 ALA B 276 ALA B 280 5 5
HELIX 33 33 PRO B 287 GLY B 303 1 17
HELIX 34 34 LEU B 304 THR B 322 1 19
HELIX 35 35 PRO B 324 GLY B 328 5 5
HELIX 36 36 GLY B 332 ILE B 346 1 15
SHEET 1 A10 ALA A 35 VAL A 38 0
SHEET 2 A10 LYS A 2 GLY A 8 1 N VAL A 3 O ALA A 35
SHEET 3 A10 ALA A 66 SER A 71 1 O ALA A 66 N ALA A 4
SHEET 4 A10 VAL A 268 PRO A 271 1 N PHE A 269 O VAL A 67
SHEET 5 A10 PRO A 258 GLY A 263 -1 O SER A 259 N GLU A 270
SHEET 6 A10 LEU A 99 LYS A 107 -1 N PHE A 100 O LEU A 262
SHEET 7 A10 ASP A 127 GLU A 133 -1 O VAL A 128 N ALA A 106
SHEET 8 A10 VAL A 232 THR A 235 1 O VAL A 233 N VAL A 131
SHEET 9 A10 HIS A 179 ASP A 184 1 O HIS A 179 N VAL A 232
SHEET 10 A10 ALA A 210 TYR A 215 1 O ALA A 210 N VAL A 180
SHEET 1 B 4 GLY A 145 MET A 146 0
SHEET 2 B 4 GLU A 150 SER A 158 -1 N TRP A 152 O GLY A 145
SHEET 3 B 4 GLU B 150 SER B 158 -1 O ALA B 151 N TYR B 157
SHEET 4 B 4 GLY B 145 MET B 146 -1 O GLY B 145 N TRP B 152
SHEET 1 C10 ALA B 35 VAL B 38 0
SHEET 2 C10 LYS B 2 GLY B 8 1 N VAL B 3 O ALA B 35
SHEET 3 C10 ALA B 66 SER B 71 1 O ALA B 66 N ALA B 4
SHEET 4 C10 VAL B 268 PHE B 269 1 O PHE B 269 N LEU B 69
SHEET 5 C10 ALA B 260 GLY B 263 -1 N SER B 261 O VAL B 268
SHEET 6 C10 LEU B 99 LYS B 107 -1 N PHE B 100 O LEU B 262
SHEET 7 C10 ASP B 127 GLU B 133 -1 O VAL B 128 N ALA B 106
SHEET 8 C10 VAL B 232 THR B 235 1 O VAL B 233 N VAL B 131
SHEET 9 C10 HIS B 179 ASP B 184 1 O HIS B 179 N VAL B 232
SHEET 10 C10 ALA B 210 TYR B 215 1 O ALA B 210 N VAL B 180
CISPEP 1 GLU A 142 PRO A 143 0 2.28
CISPEP 2 GLU B 142 PRO B 143 0 -0.75
CRYST1 55.620 84.310 72.280 90.00 103.00 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017979 0.000000 0.004151 0.00000
SCALE2 0.000000 0.011861 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014199 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
